2pw3

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[[Image:2pw3.gif|left|200px]]
[[Image:2pw3.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2pw3 |SIZE=350|CAPTION= <scene name='initialview01'>2pw3</scene>, resolution 1.56&Aring;
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The line below this paragraph, containing "STRUCTURE_2pw3", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3&#39;,5&#39;-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PDE4D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_2pw3| PDB=2pw3 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pw3 OCA], [http://www.ebi.ac.uk/pdbsum/2pw3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pw3 RCSB]</span>
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}}
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'''Structure of the PDE4D-cAMP complex'''
'''Structure of the PDE4D-cAMP complex'''
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[[Category: Robinson, H.]]
[[Category: Robinson, H.]]
[[Category: Wang, H.]]
[[Category: Wang, H.]]
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[[Category: crystal structure.]]
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[[Category: Crystal structure.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: pde4-camp complex]]
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[[Category: Pde4-camp complex]]
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[[Category: substrate specificity]]
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[[Category: Substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:53:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:41:29 2008''
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Revision as of 10:53, 4 May 2008

Image:2pw3.gif

Template:STRUCTURE 2pw3

Structure of the PDE4D-cAMP complex


Overview

Phosphodiesterases (PDEs) are key enzymes that control the cellular concentrations of the second messengers cAMP and cGMP. The mechanism for selective recognition of substrates cAMP and cGMP by individual PDE families remains a puzzle. To understand the mechanism for substrate recognition by PDE enzymes, the crystal structure of the catalytic domain of an inactive D201N mutant of PDE4D2 in complex with substrate cAMP has been determined at 1.56 A resolution. The structure shows that Gln369 forms only one hydrogen bond with the adenine of cAMP. This finding provides experimental evidence against the hypothesis of two hydrogen bonds between the invariant glutamine and the substrate cAMP in PDE4, and thus suggests that the widely circulated "glutamine switch" model is unlikely the mechanism for substrate recognition by PDEs. A structure comparison between PDE4D2-cAMP and PDE10A2-cAMP reveals an anti configuration of cAMP in PDE4D2 but syn in PDE10A2, in addition to different contact patterns of cAMP in these two structures. These observations imply that individual PDE families have their characteristic mechanisms for substrate recognition.

About this Structure

2PW3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10., Wang H, Robinson H, Ke H, J Mol Biol. 2007 Aug 10;371(2):302-7. Epub 2007 May 26. PMID:17582435 Page seeded by OCA on Sun May 4 13:53:38 2008

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